1gl6
From Proteopedia
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|PDB= 1gl6 |SIZE=350|CAPTION= <scene name='initialview01'>1gl6</scene>, resolution 2.8Å | |PDB= 1gl6 |SIZE=350|CAPTION= <scene name='initialview01'>1gl6</scene>, resolution 2.8Å | ||
|SITE= <scene name='pdbsite=GNA:Gnp+Binding+Site+For+Chain+F'>GNA</scene> | |SITE= <scene name='pdbsite=GNA:Gnp+Binding+Site+For+Chain+F'>GNA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl6 OCA], [http://www.ebi.ac.uk/pdbsum/1gl6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gl6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Gomis-Ruth, F X.]] | [[Category: Gomis-Ruth, F X.]] | ||
[[Category: Moncalian, G.]] | [[Category: Moncalian, G.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: EPE]] | ||
| - | [[Category: GNP]] | ||
[[Category: bacterial conjug protein]] | [[Category: bacterial conjug protein]] | ||
[[Category: coupling protein]] | [[Category: coupling protein]] | ||
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[[Category: type iv secretion system]] | [[Category: type iv secretion system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:46:23 2008'' |
Revision as of 17:46, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLYSABLE GTP ANALOGUE GDPNP
Overview
The transfer of DNA across membranes and between cells is a central biological process; however, its molecular mechanism remains unknown. In prokaryotes, trans-membrane passage by bacterial conjugation, is the main route for horizontal gene transfer. It is the means for rapid acquisition of new genetic information, including antibiotic resistance by pathogens. Trans-kingdom gene transfer from bacteria to plants or fungi and even bacterial sporulation are special cases of conjugation. An integral membrane DNA-binding protein, called TrwB in the Escherichia coli R388 conjugative system, is essential for the conjugation process. This large multimeric protein is responsible for recruiting the relaxosome DNA-protein complex, and participates in the transfer of a single DNA strand during cell mating. Here we report the three-dimensional structure of a soluble variant of TrwB. The molecule consists of two domains: a nucleotide-binding domain of alpha/beta topology, reminiscent of RecA and DNA ring helicases, and an all-alpha domain. Six equivalent protein monomers associate to form an almost spherical quaternary structure that is strikingly similar to F1-ATPase. A central channel, 20 A in width, traverses the hexamer.
About this Structure
1GL6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase., Gomis-Ruth FX, Moncalian G, Perez-Luque R, Gonzalez A, Cabezon E, de la Cruz F, Coll M, Nature. 2001 Feb 1;409(6820):637-41. PMID:11214325
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